Isolation, Identification, and Biological Activity Analysis of Swim Bladder Polypeptides from Acipenser schrencki

• Published in: Foods Vol. 12; no. 10; p. 1934
• Main Authors: Zu, Xiao-Yan, Liu, Wen-Bo, Xiong, Guang-Quan, Liao, Tao, Li, Hai-Lan
• Format: Journal Article
• Language: English
• Published: Switzerland MDPI AG 09.05.2023; MDPI
• Subjects: Acipenser; Acipenser schrencki; Alkaline protease; Amino acids; Angiotensin; antioxidant peptides; Antioxidants; Aquaculture; Biological activity; Bladder; Cell cycle; Collagen; Enzymes; Ethanol; Fish; Fishing; Food; Food science; Hydrophobicity; Hydroxyproline; Ions; Mass spectrometry; Membrane separation; Molecular weight; Oxidation; peptide sequence; Peptides; Peptidyl-dipeptidase A; Physicochemical properties; Polypeptides; Potassium; Proteins; Raw materials; Scientific imaging; Sequence analysis; Signal transduction; Skin; Sturgeon; Swim bladder; swim bladder polypeptides; Ultrafiltration; Ultraviolet spectra; United States > US; China; Acipenser schrencki; swim bladder polypeptides; antioxidant peptides; peptide sequence
• ISSN: 2304-8158; 2304-8158
• DOI: 10.3390/foods12101934

Swim bladder polypeptides (SBPs) of were analyzed for their antioxidant activity and physicochemical properties. The results showed the optimal enzymatic conditions were alkaline protease with a solid-to-liquid ratio of 1:20, an incubation time of 4 h, a temperature of 55 °C, and an enzyme dosage of 5000 U/g. Three different molecular weight fractions (F1, F2, and F3) were obtained via ultrafiltration. F3 (912.44-2135.82 Da) showed 77.90%, 72.15%, and 66.25% removal of O • , DPPH•, and •OH, respectively, at 10 mg/mL, which was significantly higher than the F1 and F2 fractions ( < 0.05). F3 contained proline (6.17%), hydroxyproline (5.28%), and hydrophobic amino acids (51.39%). The UV spectrum of F3 showed maximum absorption at 224 nm. Peptide sequence analysis showed that F3 contained antioxidant peptides (MFGF, GPPGPRGPPGL, and GPGPSGERGPPGPM) and exhibited inhibitory activities on angiotensin-converting enzyme and dipeptidyl peptidase III/IV (FRF, FPFL and LPGLF). F3 was considered a good raw material for obtaining bioactive peptides.